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Information on EC 5.3.1.9 - glucose-6-phosphate isomerase and Organism(s) Trypanosoma brucei brucei and UniProt Accession P13377

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EC Tree
IUBMB Comments
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates .
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Trypanosoma brucei brucei
UNIPROT: P13377
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Word Map
The taxonomic range for the selected organisms is: Trypanosoma brucei brucei
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoglucose isomerase, glucose-6-phosphate isomerase, glucose phosphate isomerase, autocrine motility factor, phosphoglucoisomerase, phosphohexose isomerase, neuroleukin, pgi/amf, amf/pgi, glucose 6-phosphate isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphoglucose isomerase
-
6-Phosphoglucose isomerase
-
-
-
-
D-Glucose-6-phosphate isomerase
-
-
-
-
D-glucose-6-phosphate ketol-isomerase
-
-
-
-
Glucose 6-phosphate isomerase
-
-
-
-
Glucose phosphate isomerase
-
-
-
-
Glucose phosphoisomerase
-
-
-
-
Glucosephosphate isomerase 2
-
-
-
-
GPI
-
-
-
-
Hexose 6-phosphate isomerase
-
-
-
-
Hexose isomerase
-
-
-
-
Hexose monophosphate isomerase
-
-
-
-
Hexose phosphate isomerase
-
-
-
-
Hexosephosphate isomerase
-
-
-
-
Isomerase, glucose phosphate
-
-
-
-
Neuroleukin
-
-
-
-
NLK
-
-
-
-
Oxoisomerase
-
-
-
-
PGI
-
-
-
-
PGI2
-
-
-
-
PGI3
-
-
-
-
PHI
-
-
-
-
Phosphoglucoisomerase
-
-
-
-
Phosphoglucose isomerase
-
-
-
-
Phosphohexoisomerase
-
-
-
-
Phosphohexomutase
-
-
-
-
Phosphohexose isomerase
-
-
-
-
Phosphosaccharomutase
-
-
-
-
SA-36
-
-
-
-
Sperm antigen-36
-
-
-
-
VEG54
-
-
-
-
Vegetative protein 54
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose-6-phosphate aldose-ketose-isomerase (configuration-inverting)
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-41-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-phosphoarabinonhydroxamic acid
competitive inhibition
Agaricic acid
irreversible inhibition
suramin
an anti-trypanosomal drug
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00005
5-phosphoarabinonhydroxamic acid
Trypanosoma brucei brucei
-
0.01
Agaricic acid
Trypanosoma brucei brucei
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48.5
purified recombinant His-tagged enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GUTat 10.1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
PGI is the second enzyme of glycolysis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PI_TRYBB
607
0
67518
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
structure and active site conformation, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme complexed with glucose 6-phosphate, by hanging drop vapor diffusion method at room temperature, 0.004 ml of protein solution with 28.4 mg/ml protein and 5 mM fructose 6-phosphate is mixed with 0.002 ml of reservoir solution containing 10% PEG 3350, 50 mM sodium citrate, and 50 mM dithiothreitol, a few days, X-ray diffraction structure determination and analysis at 1.6 A resolution. Although fructose 6-phosphate is added to the crystallization mixture, the enzyme shows bound gluose 6-phosphate at its active site in the crystals
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal ion affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
PGI might be a good target for species-specific drug design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arsenieva, D.; Appavu, B.; Mazock, G.; Jeffery, C.
Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with glucose-6-phosphate at 1.6 A resolution
Proteins
74
72-80
2009
Rattus norvegicus, Trypanosoma brucei brucei (P13377), Trypanosoma brucei brucei Treu 927 (P13377)
Manually annotated by BRENDA team